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Q9FPH3 (THA2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable low-specificity L-threonine aldolase 2

EC=4.1.2.48
Alternative name(s):
Threonine aldolase 2
Gene names
Name:THA2
Ordered Locus Names:At3g04520
ORF Names:T27C4.17
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length355 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Threonine aldolase involved in threonine degradation to glycine. May play a role in the removal of L-allo-threonine. Ref.6

Catalytic activity

L-threonine = glycine + acetaldehyde.

L-allo-threonine = glycine + acetaldehyde.

Cofactor

Pyridoxal phosphate By similarity.

Pathway

Amino-acid degradation; L-threonine degradation via aldolase pathway; acetaldehyde and glycine from L-threonine: step 1/1.

Tissue specificity

Expressed in roots, leaf vasculature and flowers. Ref.6

Disruption phenotype

Lethal albino phenotype when homozygous. Ref.6

Sequence similarities

Belongs to the threonine aldolase family.

Biophysicochemical properties

Kinetic parameters:

KM=3.8 mM for L-threonine Ref.6

Sequence caution

The sequence AAF63783.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
   LigandPyridoxal phosphate
   Molecular functionLyase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processthreonine catabolic process

Inferred from mutant phenotype Ref.6. Source: TAIR

   Molecular_functionpyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

threonine aldolase activity

Inferred from direct assay Ref.6. Source: TAIR

Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: Q9FPH3-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 355355Probable low-specificity L-threonine aldolase 2
PRO_0000428660

Amino acid modifications

Modified residue2111N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: D7D1EFDBA18B517E

FASTA35538,252
        10         20         30         40         50         60 
MVTPTTIRTV DLRSDTVTKP TESMRSAMAN AEVDDDVLGN DPTALRLEKE VAEIAGKEAA 

        70         80         90        100        110        120 
MFVPSGTMGN LISVLVHCDE RGSEVILGDD SHIHIYENGG VSSLGGVHPR TVKNEEDGTM 

       130        140        150        160        170        180 
EIGAIEAAVR SPKGDLHHPV TKLICLENTQ ANCGGRCLPI EYIDKVGELA KKHGLKLHID 

       190        200        210        220        230        240 
GARIFNASVA LGVPVKRIVQ AADSVSICLS KGIGAPVGSV IVGSKKFITK ARWLRKTLGG 

       250        260        270        280        290        300 
GMRQIGVLCA AALVALHENV AKLEDDHKKA RVLAEGLNRI ERLRVNVAAV ETNIIYVDIP 

       310        320        330        340        350 
EDPKFGAEEA CKSLEDVGVL VIPQATFRIR IVLHHQISDV DVEYVLSCFE KIFHS 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. expand/collapse author list , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"Two Arabidopsis threonine aldolases are nonredundant and compete with threonine deaminase for a common substrate pool."
Joshi V., Laubengayer K.M., Schauer N., Fernie A.R., Jander G.
Plant Cell 18:3564-3575(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC022287 Genomic DNA. Translation: AAF63783.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE74091.1.
AF325033 mRNA. Translation: AAG40385.1.
AY091093 mRNA. Translation: AAM14044.1.
AY123033 mRNA. Translation: AAM67566.1.
AK175345 mRNA. Translation: BAD43108.1.
AY085456 mRNA. Translation: AAM62682.1.
RefSeqNP_566228.1. NM_111323.3.
UniGeneAt.19145.

3D structure databases

SMRQ9FPH3. Positions 10-353.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT3G04520.1-P.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G04520.1; AT3G04520.1; AT3G04520.
GeneID819608.
KEGGath:AT3G04520.

Organism-specific databases

TAIRAT3G04520.

Phylogenomic databases

eggNOGCOG2008.
InParanoidQ9FPH3.
KOK01620.
OMAEVGDEQI.
PhylomeDBQ9FPH3.
ProtClustDBPLN02721.

Enzyme and pathway databases

BioCycARA:GQT-2165-MONOMER.
BRENDA2.1.2.1. 302.
UniPathwayUPA00044; UER00429.

Gene expression databases

GenevestigatorQ9FPH3.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR001597. ArAA_b-elim_lyase/Thr_aldolase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR023603. Threonine_aldolase.
[Graphical view]
PfamPF01212. Beta_elim_lyase. 1 hit.
[Graphical view]
PIRSFPIRSF017617. Thr_aldolase. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTHA2_ARATH
AccessionPrimary (citable) accession number: Q9FPH3
Secondary accession number(s): Q9M835
Entry history
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names